Component

Agrobacterium strain CP4 EPSP synthase

2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

  1. Potassium activated purified CP4 EPSPS, with a reported binding estimate around 25 mM.

    Potassium ion → Agrobacterium strain CP4 EPSP synthase source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally.
    experimental_contrast
    {"intervention": "K+ supplied in enzyme assay", "comparator": "Assay without activating monovalent cation", "endpoint": "Potassium activated purified CP4 EPSPS, with a reported binding estimate around 25 mM.", "effect_direction": "increase", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Purified strain CP4 enzyme; monovalent-cation comparison.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Specific bacterial enzyme, not human potassium status or a universal EPSPS gate.
    plain_language
    Potassium activated purified CP4 EPSPS, with a reported binding estimate around 25 mM.
    primary_references
    Molecular basis for the herbicide resistance of Roundup Ready crops. | 2006 | DOI 10.1073/pnas.0603638103 | PMID 16916934 | https://pubmed.ncbi.nlm.nih.gov/16916934/ | https://doi.org/10.1073/pnas.0603638103 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1559744/
    source_locator
    Reviewed reference lines 19-19; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 19–19

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Purified strain CP4 enzyme; monovalent-cation comparison. · source_derived_draft · unverified_draft

    **Potassium dependence is enzyme-specific.** The CP4 EPSPS study found activation by K+, NH4+ and Rb+; the reported K+ dissociation estimate was approximately 25 mM. This result belongs to that purified bacterial enzyme. It does not mean human potassium intake controls all EPSPS enzymes or makes glyphosate inhibition irrelevant. [Molecular basis for the herbicide resistance of Roundup Ready crops.](https://pubmed.ncbi.nlm.nih.gov/16916934/)
    Complete structured claim and evidence
  2. Glyphosate inhibited cp4-epsps with an approximate purified-enzyme IC50 of 11 millimolar.

    Glyphosate → Agrobacterium strain CP4 EPSP synthase source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally.
    experimental_contrast
    {"intervention": "Glyphosate titration", "comparator": "Enzyme without glyphosate", "endpoint": "Glyphosate inhibited cp4-epsps with an approximate purified-enzyme IC50 of 11 millimolar.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Purified enzyme comparison, Funke 2006.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    IC50 depends on assay conditions; not a growth threshold, dietary exposure limit or complete microbiome response.
    plain_language
    Glyphosate inhibited cp4-epsps with an approximate purified-enzyme IC50 of 11 millimolar.
    primary_references
    Molecular basis for the herbicide resistance of Roundup Ready crops. | 2006 | DOI 10.1073/pnas.0603638103 | PMID 16916934 | https://pubmed.ncbi.nlm.nih.gov/16916934/ | https://doi.org/10.1073/pnas.0603638103 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1559744/
    source_locator
    Reviewed reference lines 17-17; exact primary location described in quoted passage where extracted.

    Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 17–17

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Purified enzyme comparison, Funke 2006. · source_derived_draft · unverified_draft

    **EPSPS uses a second PEP molecule.** E. coli EPSPS (AroA) transfers an enolpyruvyl group from a second PEP molecule to shikimate-3-phosphate, making 5-enolpyruvylshikimate-3-phosphate (EPSP) and phosphate. Glyphosate inhibits this enzyme by occupying the PEP-associated substrate site in the substrate-bound enzyme. Purified-enzyme IC50 estimates were about 2.5 µM for E. coli EPSPS and 11 mM for CP4 EPSPS. These are not interchangeable microbial-growth thresholds or human intestinal effect concentrations. Adding shikimate upstream does not remove the need for EPSPS downstream. [Molecular basis for the herbicide resistance of Roundup Ready crops.](https://pubmed.ncbi.nlm.nih.gov/16916934/)
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.